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• W52786287 abstract "Publisher Summary That two different enzymes, catalyzing apparently concerted reactions, should exhibit different kinetic mechanisms of action is a thought-provoking problem for the practicing kineticist. For example, muscle lactate dehydrogenase exhibits an ordered sequential mechanism, while in the case of yeast hexokinase the pathway of enzyme and substrate interaction is thought to be random. For both these enzymes, the transition state is similar in the sense that it lies somewhere between enzyme-substratoi-substrate and enzyme-product-product. From the view of catalysis exclusively, however, there is no clear advantage for lactate dehydrogenase to bind its substrates in an ordered rather than a random fashion. The data for approximately 60 different enzyme systems have been summarized in which there is strong evidence for the participation of covalent enzyme substrate intermediates in catalysis. A number of ways have been listed in which such intermediates can be catalytically important, but the list also states that, considering the catalytic potential of enzymes, such intermediates are not essential for enzyme action." @default.
• W52786287 created "2016-06-24" @default.
• W52786287 creator A5023871177 @default.
• W52786287 creator A5054730579 @default.
• W52786287 date "1972-01-01" @default.
• W52786287 modified "2023-09-27" @default.
• W52786287 title "A Possible Role for Kinetic Reaction Mechanism Dependent Substrate and Product Effects in Enzyme Regulation" @default.
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• W52786287 doi "https://doi.org/10.1016/b978-0-12-152806-5.50011-4" @default.
• W52786287 hasPublicationYear "1972" @default.
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